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Literature summary extracted from

  • Meng, Z.; Liu, Z.; Lou, Z.; Gong, X.; Cao, Y.; Bartlam, M.; Zhang, K.; Rao, Z.
    Purification, characterization and crystallization of pyrroline-5-carboxylate reductase from the hyperthermophilic archeon Sulfolobus Solfataricus (2009), Protein Expr. Purif., 64, 125-130.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.2
-
 Saccharolobus solfataricus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.2 diffraction to 3.5 A resolution Saccharolobus solfataricus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.1.2 soluble
-
 Saccharolobus solfataricus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.2 30000
-
 x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes Saccharolobus solfataricus
1.5.1.2 320000
-
 gel filtration Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.2 Saccharolobus solfataricus Q97ZT3
-
-
1.5.1.2 Saccharolobus solfataricus P2 Q97ZT3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.2 recombinant enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.2 1-pyrroline-5-carboxylate + NAD(P)H
-
 Saccharolobus solfataricus L-proline + NAD(P)+
-
 r
1.5.1.2 1-pyrroline-5-carboxylate + NAD(P)H
-
 Saccharolobus solfataricus P2 L-proline + NAD(P)+
-
 r
1.5.1.2 L-proline + NAD(P)+
-
 Saccharolobus solfataricus 1-pyrroline-5-carboxylate + NAD(P)H
-
 r
1.5.1.2 L-proline + NAD(P)+
-
 Saccharolobus solfataricus P2 1-pyrroline-5-carboxylate + NAD(P)H
-
 r
1.5.1.2 L-thioproline + NAD(P)+
-
 Saccharolobus solfataricus 1-pyrroline-3-thio-5-carboxylate + NAD(P)H
-
 r
1.5.1.2 L-thioproline + NAD(P)+
-
 Saccharolobus solfataricus P2 1-pyrroline-3-thio-5-carboxylate + NAD(P)H
-
 r

Subunits

EC Number Subunits Comment Organism
1.5.1.2 multimer x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.2 70
-
 stable for at least 30 min Saccharolobus solfataricus
1.5.1.2 80
-
 half-life 30 min Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.2 7
-
 reaction rate at pH 9.0 is nearly 3fold higher than at pH 7.0 Saccharolobus solfataricus
1.5.1.2 9
-
 reaction rate is nearly 3fold higher than at pH 7.0 Saccharolobus solfataricus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.2 NAD+ 2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM Saccharolobus solfataricus
1.5.1.2 NADH
-
 Saccharolobus solfataricus
1.5.1.2 NADP+ 2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM Saccharolobus solfataricus
1.5.1.2 NADPH
-
 Saccharolobus solfataricus